Conformation of the tripeptide Cbz-Pro-Leu-Trp-OBzl(CF3)2 deduced from two-dimensional 1H-NMR and conformational energy calculations is related to its affinity for NK1-receptor
✍ Scribed by Régis Millet; Laurence Goossens; Jean-François Goossens; Philippe Chavatte; Karine Bertrand-Caumont; Raymond Houssin; Jean-Pierre Hénichart
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 895 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.326
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✦ Synopsis
Abstract
Chemical modifications of dual NK~1~/NK~2~ ligand Cbz‐Gly‐Leu‐Trp‐OBzl(CF~3~)~2~ (1) enabled us to create a high NK~1~ selective ligand Cbz‐Pro‐Leu‐Trp‐OBzl(CF~3~)~2~ (2). A determination of the conformational behavior of tripeptide 2 in solution is described. The 1D and 2D ^1^H‐NMR techniques (COSY and ROESY) were used to assign resonances. Observed interproton distance restraints were considered to characterize conformational behavior. Spectral data indicate that tripeptide 2 presents a rigidified structure in DMSO stabilized by H‐bond in two γ‐turns. Agreement with experimental data was obtained by averaging the ^1^H‐NMR parameters over several combinations of low‐energy conformations. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.